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1kok

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{{STRUCTURE_1kok| PDB=1kok | SCENE= }}
{{STRUCTURE_1kok| PDB=1kok | SCENE= }}
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'''Crystal Structure of Mesopone Cytochrome c Peroxidase (MpCcP)'''
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===Crystal Structure of Mesopone Cytochrome c Peroxidase (MpCcP)===
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==Overview==
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The effect of heme ring oxygenation on enzyme structure and function has been examined in a reconstituted cytochrome c peroxidase. Oxochlorin derivatives were formed by OsO(4) treatment of mesoporphyrin followed by acid-catalyzed pinacol rearrangement. The northern oxochlorin isomers were isolated by chromatography, and the regio-isomers assignments determined by 2D COSY and NOE 1H NMR. The major isomer, 4-mesoporphyrinone (Mp), was metallated with FeCl(2) and reconstituted into cytochrome c peroxidase (CcP) forming a hybrid green protein, MpCcP. The heme-altered enzyme has 99% wild-type peroxidase activity with cytochrome c. EPR spectroscopy of MpCcP intermediate compound I verifies the formation of the Trp(191) radical similar to wild-type CcP in the reaction cycle. Peroxidase activity with small molecules is varied: guaiacol turnover increases approximately five-fold while that with ferrocyanide is approximately 85% of native. The electron-withdrawing oxo-substitutents on the cofactor cause a approximately 60-mV increase in Fe(III)/Fe(II) reduction potential. The present investigation represents the first structural characterization of an oxochlorin protein with X-ray intensity data collected to 1.70 A. Although a mixture of R- and S-mesopone isomers of the FeMP cofactor was used during heme incorporation into the apo-protein, only the S-isomer is found in the crystallized protein.
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{{ABSTRACT_PUBMED_12237229}}
==About this Structure==
==About this Structure==
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[[Category: Proximal loop]]
[[Category: Proximal loop]]
[[Category: Trp191 cationic radical]]
[[Category: Trp191 cationic radical]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:39:34 2008''

Revision as of 07:39, 2 July 2008

Image:1kok.png

Template:STRUCTURE 1kok

Crystal Structure of Mesopone Cytochrome c Peroxidase (MpCcP)

Template:ABSTRACT PUBMED 12237229

About this Structure

1KOK is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Mesopone cytochrome c peroxidase: functional model of heme oxygenated oxidases., Immoos CE, Bhaskar B, Cohen MS, Barrows TP, Farmer PJ, Poulos TL, J Inorg Biochem. 2002 Sep 20;91(4):635-43. PMID:12237229

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